Derivative of mouse TGF-beta2, with a deletion of residues 52-71 and K25R, R26K, L51R, A74K, C77S, L89V, I92V, K94R T95K, I98V single amino acid substitutions, bound to human TGF-beta type II receptor ectodomain residues 15-130. Determined by X-ray diffraction at 1.88 Å resolution. Released 1 Mar 2017.
Explore 5TX4 in 3D Show helices and sheets RCSB PDB PDBe
5TX4 contains 4 α-helices and 26 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-26 | 4 | |
| β-strand | 27-29 | 3 | 1 |
| β-strand | 32-35 | 4 | 2 |
| β-strand | 43-45 | 3 | 3 |
| β-strand | 51-53 | 3 | 1 |
| β-strand | 60-67 | 8 | 2 |
| β-strand | 72-79 | 8 | 2 |
| β-strand | 85 | 1 | 4 |
| β-strand | 88 | 1 | 4 |
| β-strand | 98-99 | 2 | 3 |
| β-strand | 101-105 | 5 | 2 |
| β-strand | 108-115 | 8 | 2 |
| α-helix | 120-122 | 3 | |
| β-strand | 123-125 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 5 |
| α-helix | 4-9 | 6 | |
| β-strand | 14 | 1 | 6 |
| β-strand | 16-18 | 3 | 7 |
| β-strand | 21-23 | 3 | 8 |
| α-helix | 24-28 | 5 | |
| β-strand | 33-35 | 3 | 1 |
| β-strand | 38-40 | 3 | 8 |
| β-strand | 43-45 | 3 | 7 |
| β-strand | 47 | 1 | 6 |
| β-strand | 51 | 1 | 9 |
| β-strand | 54 | 1 | 9 |
| β-strand | 58-60 | 3 | 5 |
| β-strand | 63-72 | 10 | 1 |
| β-strand | 75-86 | 12 | 1 |
| β-strand | 88-91 | 4 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| TGF-beta receptor type-2 | A | protein | 116 | Homo sapiens | P37173 (AlphaFold model) |
| Transforming growth factor beta-2 | B | protein | 92 | Homo sapiens | P61812 (AlphaFold model) |
>5TX4_1 TGF-beta receptor type-2 (chains A) VTDNNGAVKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITL ETVCHDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEY
>5TX4_2 Transforming growth factor beta-2 (chains B) ALDAAYCFRNVQDNCCLRPLYIDFRKDLGWKWIHEPKGYNANFCAGACPYRASKSPSCVS QDLEPLTIVYYVGRKPKVEQLSNMIVKSCKCS
An engineered transforming growth factor beta (TGF-beta ) monomer that functions as a dominant negative to block TGF-beta signaling. Kim, S.K., Barron, L., Hinck, C.S. et al. J Biol Chem (2017) 292:7173-7188. DOI 10.1074/jbc.M116.768754 · PubMed
Other PDB entries of the same protein (UniProt P37173 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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